Education
- PhD, 1966, MIT
Research Summary
Paul Schimmel’s research interests have focused on aminoacyl tRNA synthetases — an ancient and universal set of essential enzymes. His laboratory has worked on a universal mechanism for correcting errors in the interpretation of genetic information, and went on to show how this mechanism is essential for maintaining cellular homeostasis and preventing serious pathologies and disease. His laboratory also discovered what others refer to as a ‘tRNA synthetase-directed primordial’ or ‘second’ genetic code, which was eventually incorporated into the modern code. In a separate line of research published back in 1983, Schimmel developed the concept of what are now known as ESTs (expressed sequence tags), and the strategy of shotgun sequencing — approaches that were adopted into the human genome project several years later. Lastly, his laboratory connected synthetases to disease and, most recently, they reported the structural and functional metamorphosis of these proteins, whereby they are repurposed with novel activities, both inside and outside the cell, in a variety of cell signaling pathways. The Schimmel lab is no longer accepting students.Awards
- Member of the American Academy of Arts and Sciences
- Member of the National Academy of Sciences
- Member of the American Philosophical Society
- Member of the Institute of Medicine (National Academy of Medicine)
- Member of the National Academy of Inventors
- Former President of the Division of Biological Chemistry of the American Chemical Society
- Editorial board member on numerous scientific journals
Recent Publications
- Metabolic regulation of mRNA splicing. Cui, H, Shi, Q, Macarios, CM, Schimmel, P. 2024. Trends Cell Biol 34, 756-770.
doi: 10.1016/j.tcb.2024.02.002PMID:38431493 - tRNA renovatio: Rebirth through fragmentation. Kuhle, B, Chen, Q, Schimmel, P. 2023. Mol Cell 83, 3953-3971.
doi: 10.1016/j.molcel.2023.09.016PMID:37802077 - Structural basis for a degenerate tRNA identity code and the evolution of bimodal specificity in human mitochondrial tRNA recognition. Kuhle, B, Hirschi, M, Doerfel, LK, Lander, GC, Schimmel, P. 2023. Nat Commun 14, 4794.
doi: 10.1038/s41467-023-40354-2PMID:37558671 - Publisher Correction: Arg-tRNA synthetase links inflammatory metabolism to RNA splicing and nuclear trafficking via SRRM2. Cui, H, Diedrich, JK, Wu, DC, Lim, JJ, Nottingham, RM, Moresco, JJ, Yates, JR 3rd, Blencowe, BJ, Lambowitz, AM, Schimmel, P et al.. 2023. Nat Cell Biol 25, 1073.
doi: 10.1038/s41556-023-01172-2PMID:37237245 - Arg-tRNA synthetase links inflammatory metabolism to RNA splicing and nuclear trafficking via SRRM2. Cui, H, Diedrich, JK, Wu, DC, Lim, JJ, Nottingham, RM, Moresco, JJ, Yates, JR 3rd, Blencowe, BJ, Lambowitz, AM, Schimmel, P et al.. 2023. Nat Cell Biol 25, 592-603.
doi: 10.1038/s41556-023-01118-8PMID:37059883 - Structural basis for shape-selective recognition and aminoacylation of a D-armless human mitochondrial tRNA. Kuhle, B, Hirschi, M, Doerfel, LK, Lander, GC, Schimmel, P. 2022. Nat Commun 13, 5100.
doi: 10.1038/s41467-022-32544-1PMID:36042193 - Regulation of ex-translational activities is the primary function of the multi-tRNA synthetase complex. Cui, H, Kapur, M, Diedrich, JK, Yates, JR, Ackerman, SL, Schimmel, P. 2021. Nucleic Acids Res 49, 3603-3616.
doi: 10.1093/nar/gkaa1183PMID:33341895 - Relaxed sequence constraints favor mutational freedom in idiosyncratic metazoan mitochondrial tRNAs. Kuhle, B, Chihade, J, Schimmel, P. 2020. Nat Commun 11, 969.
doi: 10.1038/s41467-020-14725-yPMID:32080176 - The endless frontier of tRNA synthetases. Schimmel, P. 2020. Enzymes 48, 1-10.
doi: 10.1016/bs.enz.2020.09.001PMID:33837700 - Serum-circulating His-tRNA synthetase inhibits organ-targeted immune responses. Adams, RA, Fernandes-Cerqueira, C, Notarnicola, A, Mertsching, E, Xu, Z, Lo, WS, Ogilvie, K, Chiang, KP, Ampudia, J, Rosengren, S et al.. 2021. Cell Mol Immunol 18, 1463-1475.
doi: 10.1038/s41423-019-0331-0PMID:31797905
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